Rapid Chemically Induced Changes of PtdIns(4,5)P 2 Gate KCNQ Ion Channels | Zendy

ByungChang Suh | Zendy; Takanari Inoue | Zendy; Tobias Meyer | Zendy; Bertil Hille | Zendy

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Rapid Chemically Induced Changes of PtdIns(4,5)P ₂ Gate KCNQ Ion Channels

Author(s) -

ByungChang Suh,

Takanari Inoue,

Tobias Meyer,

Bertil Hille

Publication year - 2006

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.1131163

Subject(s) - second messenger system , phosphatidylinositol , diacylglycerol kinase , inositol , phospholipase c , phosphatidylinositol 4,5 bisphosphate , chemistry , ion channel , microbiology and biotechnology , phosphoinositide phospholipase c , biophysics , pi , signal transduction , biochemistry , biology , protein kinase c , receptor

To resolve the controversy about messengers regulating KCNQ ion channels during phospholipase C-mediated suppression of current, we designed translocatable enzymes that quickly alter the phosphoinositide composition of the plasma membrane after application of a chemical cue. The KCNQ current falls rapidly to zero when phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2 or PI(4,5)P2] is depleted without changing Ca2+, diacylglycerol, or inositol 1,4,5-trisphosphate. Current rises by 30% when PI(4,5)P2 is overproduced and does not change when phosphatidylinositol 3,4,5-trisphosphate is raised. Hence, the depletion of PI(4,5)P2 suffices to suppress current fully, and other second messengers are not needed. Our approach is ideally suited to study biological signaling networks involving membrane phosphoinositides.

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